QUANTITATIVE REDOX SCANNING OF TISSUE SAMPLES USING A CALIBRATION PROCEDURE

HE N. XU; BAOHUA WU; SHOKO NIOKA; BRITTON CHANCE; LIN Z. LI

[1] I. E. Scheffler, Mitochondria, John Wiley and Sons, Inc., Hoboken, New Jersey (2008).

[2] A. L. Lehninger, D. L. Nelson, M. M. Cox, Principles of Biochemistry, Worth Publishers, New York (1993).

[3] B. Chance, G. R. Williams, “Method for the localization of sites for oxidative phosphorylation,” Nature 176, 250–254 (1955).

[4] J. V. Rocheleau, W. S. Head, D. W. Piston, “Quantitative NAD(P)H/flavoprotein autofluorescence imaging reveals metabolic mechanisms of pancreatic islet pyruvate response,” J. Biol. Chem. 279, 31780–31787 (2004).

[5] Y. Yuan, Y. F. Li, B. D. Cameron, P. Relue, “Fluorescence anisotropy of cellular NADH as a tool to study different metabolic properties of human melanocytes and melanoma cells,” IEEE J. Sel. Top. Quant. Electron. 13, 1671–1679 (2007).

[6] Z. Zhang, D. Blessington, H. Li, T. M. Busch, J. Glickson, Q. Luo, B. Chance, G. Zheng, “Redox ratio of mitochondria as an indicator for the response of photodynamic therapy,” J. Biomed. Opt. 9, 772–778 (2004).

[7] A. Mayevsky, B. Chance, “Oxidation-reduction states of NADH in vivo: From animals to clinical use,” Mitochondrion 7, 330–339 (2007).

[8] E. M. C. Hillman, “Optical brain imaging in vivo: Techniques and applications from animal to man,” J. Biomed. Opt. 12, 051402 (2007).

[9] K. Shibuki, R. Hishida, H. Murakami, M. Kudoh, T. Kawaguchi, M. Watanabe, S. Watanabe, T. Kouuchi, R. Tanaka, “Dynamic imaging of somatosensory cortical activity in the rat visualized by flavoprotein autofluorescence,” J. Physiol. London 549, 919–927 (2003).

[10] B. Weber, C. Burger, M. T. Wyss, G. K. von Schulthess, F. Scheffold, A. Buck, “Optical imaging of the spatiotemporal dynamics of cerebral blood flow and oxidative metabolism in the rat barrel cortex,” Eur. J. Neurosci. 20, 2664–2670 (2004).

[11] A. Mayevsky, G. G. Rogatsky, “Mitochondrial function in vivo evaluated by NADH fluorescence: From animal models to human studies,” Am. J. Physiol. Cell Physiol. 292, C615–C640 (2007).

[12] I. Hassinen, B. Chance, “Oxidation-reduction properties of the mitochondrial flavoprotein chain,” Biochem. Biophys. Res. Commun. 31, 895–900 (1968).

[13] B. Chance, B. Schoener, R. Oshino, F. Itshak, Y. Nakase, “Oxidation-reduction ratio studies of mitochondria in freeze-trapped samples. NADH and flavoprotein fluorescence signals,” J. Biol. Chem. 254, 4764–4771 (1979).

[14] B. Chance, P. Cohen, F. Jobsis, B. Schoener, “Localized fluorometry of oxidation-reduction states of intracellular pyridine nucleotide in brain and kidney cortex of the anesthetized rat,” Science 136, 325 (1962).

[15] B. Chance, N. Oshino, T. Sugano, A. Mayevsky, “Basic principles of tissue oxygen determination from mitochondrial signals,” Adv. Exp. Med. Biol. 37A, 277–292 (1973).

[16] B. Chance, “Optical method,” Annu. Rev. Biophys. Biophys. Chem. 20, 1–28 (1991).

[17] R. Banerjee, Redox Biochemistry, John Wiley and Sons, Hoboken, New Jersey (2008).

[18] M. R. Hayden, J. R. Sowers, “Redox imbalance in diabetes,” Antioxid. Redox Signal. 9, 865–867 (2007).

[19] Y. Ido, “Pyridine nucleotide redox abnormalities in diabetes,” Antioxid. Redox Signal. 9, 931–942 (2007).

[20] H. N. Xu, R. Zhou, S. Nioka, B. Chance, J. D. Glickson, L. Z. Li, “Histological basis of MR/optical imaging of human melanoma mouse xenografts spanning a range of metastatic potentials,” Adv. Exp. Med. Biol. 645, 247–253 (2009).

[21] L. Z. Li, R. Zhou, T. Zhong, L. Moon, E. J. Kim, H. Qiao, S. Pickup, M. J. Hendrix, D. Leeper, B. Chance, J. D. Glickson, “Predicting melanoma metastatic potential by optical and magnetic resonance imaging,” Adv. Exp. Med. Biol. 599, 67–78 (2007).

[22] L. Z. Li, R. Zhou, H. N. Xu, L. Moon, T. Zhong, E. J. Kim, H. Qiao, R. Reddy, D. Leeper, B. Chance, J. D. Glickson, “Quantitative magnetic resonance and optical imaging biomarkers of melanoma metastatic potential,” Proc. Natl. Acad. Sci. USA 106, 6608–6613 (2009).

[23] B. Chance, B. Schoener, R. Oshino, F. Itshak, Y. Nakase, “Oxidation-reduction ratio studies of mitochondria in freeze-trapped samples. NADH and flavoprotein fluorescence signals,” J. Biol. Chem. 254, 4764–4771 (1979).

[24] B. Quistorff, J. C. Haselgrove, B. Chance, “High spatial resolution readout of 3D metabolic organ structure: An automated, low-temperature redox ratio-scanning instrument,” Anal. Biochem. 148, 389–400 (1985).

[25] Y. Gu, Z. Qian, J. Chen, D. Blessington, N. Ramanujam, B. Chance, “High-resolution threedimensional scanning optical image system for intrinsic and extrinsic contrast agents in tissue,” Revi. Sci. Instrum. 73, 172–178 (2002).

[26] L. Z. Li, H. N. Xu, M. Ranji, S. Nioka, B. Chance, “Mitochondrial redox imaging for cancer diagnostic and therapeutic studies,” J. Innov. Opt. Health Sci., 2, 325–341 (2009).

[27] M. Ranji, S. Nioka, H. N. Xu, B. Wu, L. Z. Li, D. L. Jaggard, B. Chance, “Fluorescent images of mitochondrial redox states in in situ mouse hypoxic ischemic intestines,” J. Innov. Opt. Health Sci. 2, 365–374 (2009).

[28] H. N. Xu, B. Wu, S. Nioka, B. Chance, L. Z. Li, Calibration of redox scanning for tissue samples, Biomedical Optics 71742F (SPIE, San Jose, CA (2009)).

[29] J. V. Passonneau, O. H. Lowry, Enzymatic Analysis: A Practical Guide, Humana Press, Totowa, NJ (1993).

[30] Y. Avi-Dor, J. M. Olson, M. D. Doherty, N. O. Kaplan, “Fluorescence of pyridine nucleotides in mitochondria,” J. Biol. Chem. 237, 2377–2383 (1962).

[31] M. Wakita, G. Nishimura, M. Tamura, “Some characteristics of the fluorescence lifetime of reduced pyridine nucleotides in isolated mitochondria, isolated hepatocytes, and perfused rat liver in situ,” J. Biochem. 118, 1151–1160 (1995).

[32] A. K. Ghosh, D. Finegold, W. White, K. Zawalich, F. M. Matschinsky, “Quantitative histochemical resolution of the oxidation-reduction and phosphate potentials within the simple hepatic acinus,” J. Biol. Chem. 257, 5476–5481 (1982).

[33] R. S. Bradley, M. S. Thorniley, “A review of attenuation correction techniques for tissue fluorescence,” J. R. Soc. Interface 3, 1–13 (2006).

[34] P. Balogh, G. Horvath, A. K. Szakal, “Immunoarchitecture of distinct reticular fibroblastic domains in the white pulp of mouse spleen,” J. Histochem. Cytochem. 52, 1287–1298 (2004).

[35] S. Zhuo, J. Chen, T. Luo, X. Jiang, S. Xie, R. Chen, “Two-layered multiphoton microscopic imaging of cervical tissue,” Lasers Med. Sci. 24, 359–363 (2009).

[36] L. M. Tiede, S. M. Rocha-Sanchez, R. Hallworth, M. G. Nichols, K. Beisel, “Determination of hair cell metabolic state in isolated cochlear preparations by two-photon microscopy,” J. Biomed. Opt. 12, 021004 (2007).

[37] M. C. Skala, K.M. Riching, A. Gendron-Fitzpatrick, J. Eickhoff, K. W. Eliceiri, J. G. White, N. Ramanujam, “In vivo multiphoton microscopy of NADH and FAD redox states, fluorescence lifetimes, and cellular morphology in precancerous epithelia,” Proc. Natl. Acad. Sci. USA 104, 19494–19499 (2007).

[38] S. Zhuo, J. Chen, N. Cao, X. Jiang, S. Xie, S. Xiong, “Imaging collagen remodeling and sensing transplanted autologous fibroblast metabolism in mouse dermis using multimode nonlinear optical imaging,” Phys. Med. Biol. 53, 3317–3325 (2008).

[39] J. G. Lyubovitsky, J. A. Spencer, T. B. Krasieva, B. Andersen, B. J. Tromberg, “Imaging corneal pathology in a transgenic mouse model using nonlinear microscopy,” J. Biomed. Opt. 11, 014013 (2006).

[40] S. Huang, A. A. Heikal, W. W. Webb, “Twophoton fluorescence spectroscopy and microscopy of NAD(P)H and flavoprotein,” Biophys. J. 82, 2811– 2825 (2002).